Abstract
Effect of pH on the conformational behaviour of ficin (EC 3.4.22.3), a cysteine protease from the latex of Ficus carica was monitored by circular dichroism, fluorescence spectroscopy, ANS binding and hydrodynamic studies. The results obtained from near- and far-UV CD, intrinsic fluorescence and ANS binding studies demonstrate that ficin exhibits the characteristic properties of molten globule at acidic conditions between pH 1.4 and 2.0. Ficin at pH 1.4 retained about ∼74% secondary structure with a substantial loss of tertiary structure. The acid-induced state was found to have a compact shape as measured by Stokes radius on size exclusion chromatography.
| Original language | English |
|---|---|
| Pages (from-to) | 248-254 |
| Number of pages | 7 |
| Journal | International Journal of Biological Macromolecules |
| Volume | 45 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - 1 Oct 2009 |
| Externally published | Yes |
Keywords
- Acid-unfolding
- Cysteine protease
- Ficin
- Molten globule
- Protein folding
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